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Molecular characteristics of the transferrin-receptor complex of the rabbit reticulocyte

โœ Scribed by Hu, Hsiang-Yun Yang ;Aisen, Philip


Book ID
102926535
Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
723 KB
Volume
8
Category
Article
ISSN
0091-7419

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โœฆ Synopsis


A macromolecular complex of transferrin and a membrane component was isolated by gel filtration chromatography from Triton X-1 00-solubilized ghosts of reticulocytes previously incubated with 125 I-labeled transfenin. This complex is believed to be transferrin specifically associated with its primary receptor. Following the procedures of Clark [ 141, the complex in Triton X-100 was found to behave as an asymmetric molecule with a molecular weight of approximately 250,000 and an axial ratio of 9: 1. On SDS-polyacrylamide gel electrophoresis the complex displays, in addition to transferrin, components of molecular weights 176,000 and 95,000, respectively. The larger component may be a dimer of the smaller. Each appears to crosslink, with dimethyl suberimidate, to transferrin. These results are compatible with the hypothesis that the transferrin receptor itself has a molecular weight near 175,000 and may be a dimer of two smaller components each of molecular weight near 95,000,


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